| IED ID | IndEnz0002006516 |
| Enzyme Type ID | protease006516 |
| Protein Name |
Matrix metalloproteinase-19 MMP-19 EC 3.4.24.- Matrix metalloproteinase RASI Matrix metalloproteinase-18 MMP-18 |
| Gene Name | MMP19 MMP18 RASI |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MNCQQLWLGFLLPMTVSGRVLGLAEVAPVDYLSQYGYLQKPLEGSNNFKPEDITEALRAFQEASELPVSGQLDDATRARMRQPRCGLEDPFNQKTLKYLLLGRWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGAADIRLSFHGRQSSYCSNTFDGPGRVLAHADIPELGSVHFDEDEFWTEGTYRGVNLRIIAAHEVGHALGLGHSRYSQALMAPVYEGYRPHFKLHPDDVAGIQALYGKKSPVIRDEEEEETELPTVPPVPTEPSPMPDPCSSELDAMMLGPRGKTYAFKGDYVWTVSDSGPGPLFRVSALWEGLPGNLDAAVYSPRTQWIHFFKGDKVWRYINFKMSPGFPKKLNRVEPNLDAALYWPLNQKVFLFKGSGYWQWDELARTDFSSYPKPIKGLFTGVPNQPSAAMSWQDGRVYFFKGKVYWRLNQQLRVEKGYPRNISHNWMHCRPRTIDTTPSGGNTTPSGTGITLDTTLSATETTFEY |
| Enzyme Length | 508 |
| Uniprot Accession Number | Q99542 |
| Absorption | |
| Active Site | ACT_SITE 213; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by TIMP-2, TIMP-3 and TIMP-4, while TIMP-1 is less efficient. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin. {ECO:0000269|PubMed:10809722, ECO:0000269|PubMed:10922468}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (7); Chain (1); Disulfide bond (1); Erroneous translation (1); Glycosylation (1); Metal binding (4); Motif (1); Mutagenesis (2); Natural variant (4); Propeptide (1); Region (1); Repeat (4); Sequence conflict (1); Signal peptide (1) |
| Keywords | Alternative splicing;Angiogenesis;Calcium;Collagen degradation;Developmental protein;Differentiation;Direct protein sequencing;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Activated by autolytic cleavage after Lys-97.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000269|PubMed:25171405}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10986281; 12684035; 15241558; 15868410; 16825321; 1698775; 18617639; 19812315; 20142769; 20711500; 2253219; 3095317; 3223920; 7547873; 8920930; 9065415; 9115292; 9428515; |
| Motif | MOTIF 83..90; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 57,357 |
| Kinetics | |
| Metal Binding | METAL 85; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 212; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 216; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 222; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |